{PDOC51170}
{PS51170; CW}
{BEGIN}
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* Cell wall-binding repeat profile *
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The  cell  wall-binding  repeat  (CW)   is  a  ~20  amino  acid residue module
essentially  found  in  two  bacterial Gram-positive protein families: choline
binding  proteins  and  glucosyltransferases  (EC 2.4.1.5). In choline-binding
proteins  cell  wall binding repeats bind to choline moieties of both teichoic
and  lipoteichoic  acids,  two  components  peculiar  to  the  cell surface of
Gram-positive  bacteria [1,2]. In glucosyltransferases the region spanning the
CW repeats is a glucan binding domain [3].

Several  crystal  structures  of  CW  have  been  solved [4,5]. In the choline
binding  protein  LytA  (see  <PDB:1HCX>),  the  repeats adopt a solenoid fold
consisting  exclusively  of  beta-hairpins  that  stack  to form a left-handed
superhelix  with  a  boomerang-like  shape.  The  choline  groups bind between
beta-hairpin  'steps'  of  the superhelix [4]. In Cpl-1 CW repeats assemble in
two sub-domains: an N-terminal superhelical moiety similar to the LytA one and
a  C-terminal  beta-sheet  involved  in interactions with the lysozyme domain.
Choline  is  bound  between  repeats 1 and 2, and, 2 and 3 of the superhelical
sub-domain [5].

Some proteins known to contain cell-wall binding repeats:

 - Pneumococcal   N-acetylmuramoyl-L-alanine  amidase  (autolysin,  lytA)  (EC
   3.5.1.28).  It  is a surface-exposed enzyme that rules the self-destruction
   of  pneumococcal cells through degradation of their peptidoglycan backbone.
   It mediates the release of toxic substances that damage the host tissues.
 - Pneumococcal  endo-beta-N-acetylglucosaminidase  (lytB)  (EC  3.2.1.96). It
   plays an important role in cell wall degradation and cell separation
 - Pneumococcal teichoic acid phosphorylcholine esterase (pce or cbpE), a cell
   wall hydrolase important for cellular adhesion and colonisation.
 - Lactobacillales  glucosyltransferase. It catalyzes the transfer of glucosyl
   units from the cleavage of sucrose to a growing chain of glucan.
 - Clostridium  difficile  toxin  A  (tcdA)  and  toxin B (tcdb). They are the
   causative  agents  of  the  antibiotic-associated pseudomembranous colitis.
   They  are  intracellular  acting  toxins  that  reach  their  targets after
   receptor-mediated endocytosis.
 - Clostridium acetobutylicum cspA protein.
 - Siphoviridae  bacteriophages  N-acetylmuramoyl-L-alanine  amidase. It lyses
   the bacterial host cell wall.
 - Podoviridae  lysozyme  protein  (cpl-1).  It  is  capable  of digesting the
   pneumococcal cell wall.

The profile we developed covers the 20 amino acids of the CW repeat.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Note:  The  cell  wall  binding repeats are also known as the choline-binding
 repeats (ChBr) or the choline-binding domain (ChBD).

-Last update: December 2005 / First entry.

[ 1] Garcia-Bustos J.F., Tomasz A.
     "Teichoic acid-containing muropeptides from Streptococcus pneumoniae
     as substrates for the pneumococcal autolysin."
     J. Bacteriol. 169:447-453(1987).
     PubMed=2879828
[ 2] Lopez R., Garcia E.
     "Recent trends on the molecular biology of pneumococcal capsules,
     lytic enzymes, and bacteriophage."
     FEMS. Microbiol. Rev. 28:553-580(2004).
     PubMed=15539074; DOI=10.1016/j.femsre.2004.05.002
[ 3] Shah D.S., Joucla G., Remaud-Simeon M., Russell R.R.
     "Conserved repeat motifs and glucan binding by glucansucrases of oral
     streptococci and Leuconostoc mesenteroides."
     J. Bacteriol. 186:8301-8308(2004).
     PubMed=15576779; DOI=10.1128/JB.186.24.8301-8308.2004
[ 4] Fernandez-Tornero C., Lopez R., Garcia E., Gimenez-Gallego G.,
     Romero A.
     "A novel solenoid fold in the cell wall anchoring domain of the
     pneumococcal virulence factor LytA."
     Nat. Struct. Biol. 8:1020-1024(2001).
     PubMed=11694890; DOI=10.1038/nsb724
[ 5] Hermoso J.A., Monterroso B., Albert A., Galan B., Ahrazem O.,
     Garcia P., Martinez-Ripoll M., Garcia J.L., Menendez M.
     "Structural basis for selective recognition of pneumococcal cell wall
     by modular endolysin from phage Cp-1."
     Structure 11:1239-1249(2003).
     PubMed=14527392

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